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ESSENTIAL NMR is a set of lecture notes for scientists and engineers who want to brush up on their knowledge of NMR. This book is also a compendium for graduate and postgraduate students of physics and chemistry as well as for their teachers, covering all fields of NMR, i.e. NMR methodology and hardware, chemical analysis, 2D-spectroscopy, NMR imaging, flow NMR, and quality control NMR. The material, selected and organized for a one-semester course, is presented with pairs of pages addressing particular topics. One page of each pair provides a text containing the key information, the other page shows a color illustration. This is the most comprehensive textbook on NMR to date. The book is intended for beginning graduate students and doctoral students of Physics, Chemistry, Chemical Engineering, and Material Science.

Nuclear magnetic resonance --- Nuclear magnetic resonance spectroscopy

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Magnetic Resonance Spectroscopy. --- Nuclear magnetic resonance.

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Nuclear Magnetic Resonance is a powerful tool, especially for the identification of 1 13 hitherto unknown organic compounds. H- and C-NMR spectroscopy is known and applied by virtually every synthetically working Organic Chemist. Con- quently, the factors governing the differences in chemical shift values, based on chemical environment, bonding, temperature, solvent, pH, etc. , are well understood, and specialty methods developed for almost every conceivable structural challenge. Proton and carbon NMR spectroscopy is part of most bachelors degree courses, with advanced methods integrated into masters degree and other graduate courses. In view of this universal knowledge about proton and carbon NMR spectr- copy within the chemical community, it is remarkable that heteronuclear NMR is still looked upon as something of a curiosity. Admittedly, most organic compounds contain only nitrogen, oxygen, and sulfur atoms, as well as the obligatory hydrogen and carbon atoms, elements that have an unfavourable isotope distribution when it comes to NMR spectroscopy. Each of these three elements has a dominant isotope: 14 16 32 16 32 N (99. 63% natural abundance), O (99. 76%), and S (95. 02%), with O, S, and 34 14 S (4. 21%) NMR silent. N has a nuclear moment I = 1 and a sizeable quadrupolar moment that makes the NMR signals usually very broad and dif cult to analyse.

Chemistry. --- Organic Chemistry. --- Organometallic Chemistry. --- Analytical Chemistry. --- Inorganic Chemistry. --- Polymer Sciences. --- Catalysis. --- Analytical biochemistry. --- Chemistry, inorganic. --- Chemistry, Organic. --- Polymers. --- Chimie --- Biochimie analytique --- Chimie organique --- Polymères --- Catalyse --- Electronic books. -- local. --- Nuclear magnetic resonance spectroscopy. --- Phosphorimetry. --- Biochemistry --- Analytical Chemistry --- Chemistry --- Physical Sciences & Mathematics --- Luminescence analysis --- Phosphorescence analysis --- Phosphorimetric analysis --- NMR spectroscopy --- Spectroscopy, NMR --- Spectroscopy, Nuclear magnetic resonance --- Analytical chemistry. --- Inorganic chemistry. --- Organic chemistry. --- Organometallic chemistry. --- Nuclear spectroscopy --- Knight shift --- Chemistry, Analytic --- Activation (Chemistry) --- Chemistry, Physical and theoretical --- Surface chemistry --- Polymere --- Polymeride --- Polymers and polymerization --- Macromolecules --- Inorganic chemistry --- Inorganic compounds --- Analytic biochemistry --- Organic chemistry --- Bioanalytic chemistry --- Bioanalytical chemistry --- Analytical chemistry --- Ressonància magnètica nuclear. --- Compostos orgànics --- Síntesi. --- Organometallic chemistry . --- Polymers  . --- Analysis, Chemical --- Analytic chemistry --- Chemical analysis --- Chemistry, Organometallic --- Metallo-organic chemistry --- Chemistry, Organic --- Organometallic chemistry  --- Polymers   --- Catalysis

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Speci?c binding of a ligand to a receptor is a key step in a variety of biol- ical processes, such as immune reactions, enzyme cascades, or intracellular transport processes. The ligand-receptor terminology implies that the rec- tor molecule is signi?cantly larger than the ligand, and the term bioactive conformation  usually characterizes the conformation of a ligand when it is bound to a receptor. In a more general sense, bioactive conformation applies toanymoleculeinabiologicallyrelevantboundstateregardlessofsizecons- erations. Mostofthecontributions tothisbookaddressligandsthat aremuch smaller than their receptors. X-ray crystallography and high resolution NMR spectroscopy are the two main experimental techniques used to study bioactive conformations. The- fore,the twovolumes ofthisbookcover approachesthat use either ofthetwo techniques, or a combination thereof. The combination of X-ray crystallog- phy and NMR spectroscopy is particularly useful when a crystal structure of areceptorprotein,butnotofthereceptorprotein-ligandcomplex,isavailable. Anumberofexperimentaltechniquestoanalyzethebioactiveconformationof aligandwithNMRarebasedontheobservationoftheresonancesignalsofthe free ligand that is in exchange with the bound ligand. Several chapters focus onsuchapproachesthat rangefromclassical transferredNOEexperiments, totransferred dipolar couplings,toSTD (saturation transfer difference) NMR techniques. Incaseswhere tightbinding inthesub-nanomolar rangeprevents the analysis of the bioactive conformation via free ligand signals, the ligand- proteincomplexhas tobeanalyzed withproteinNMR-based techniques orby crystallography.Sincethisareahasbeenthesubjectofmanyreviewsandmo- graphsitwill not be covered here in particular detail. As a unifying theme, all contributionstargetthequestionofhowmolecular recognitionofbiologically active molecules is achieved on the atomic scale. Depending on the research topic the results from these studies have a strong impact not only in basic research but also in several ?elds of application ranging frompharmaceutical applications tothe use of biomolecules as, for example, cryoprotectants.

Chemistry. --- Organic Chemistry. --- Biochemistry, general. --- Physical Chemistry. --- Medicinal Chemistry. --- Analytical Chemistry. --- Analytical biochemistry. --- Chemistry, Organic. --- Physical organic chemistry --- Biochemistry. --- Chimie --- Biochimie analytique --- Chimie organique --- Chimie organique physique --- Biochimie --- Conformational analysis --- Bioactive compounds --- Ligand binding (Biochemistry) --- Molecular Conformation --- Binding Sites --- Ligands --- Nuclear Magnetic Resonance, Biomolecular --- Protein Binding --- Analysis --- Chemistry --- Biochemistry --- Physical Sciences & Mathematics --- 577.354.3 --- Chemoreception --- 577.354.3 Chemoreception --- Conformational analysis. --- Analysis. --- Binding, Ligand (Biochemistry) --- Analysis, Conformational --- Biologically active compounds --- Compounds, Bioactive --- Compounds, Biologically active --- Compounds, Physiologically active --- Physiologically active compounds --- Analytical chemistry. --- Organic chemistry. --- Physical chemistry. --- Medicinal chemistry. --- Dye-ligand affinity chromatography --- Radioligand assay --- Molecular rotation --- Chemicals --- Chemistry, Physical organic. --- Analytic biochemistry --- Chemistry, Analytic --- Chemistry, Physical organic --- Chemistry, Organic --- Chemistry, Physical and theoretical --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Medical sciences --- Organic chemistry --- Composition --- Bioanalytic chemistry --- Bioanalytical chemistry --- Analytical chemistry --- Analysis, Chemical --- Analytic chemistry --- Chemical analysis --- Chemistry, Medical and pharmaceutical --- Chemistry, Pharmaceutical --- Drug chemistry --- Drugs --- Medical chemistry --- Medicinal chemistry --- Pharmacochemistry --- Chemistry, Theoretical --- Physical chemistry --- Theoretical chemistry --- Bioactive compounds - Analysis